 |
PDBsum entry 1ftt
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
DNA binding protein
|
PDB id
|
|
|
|
1ftt
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
|
Eur J Biochem
241:101-113
(1996)
|
|
PubMed id:
|
|
|
|
|
| |
|
Analysis of the solution structure of the homeodomain of rat thyroid transcription factor 1 by 1H-NMR spectroscopy and restrained molecular mechanics.
|
|
G.Esposito,
F.Fogolari,
G.Damante,
S.Formisano,
G.Tell,
A.Leonardi,
R.Di Lauro,
P.Viglino.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
The solution structure of the rat thyroid transcription factor 1 (TTF-1)
homeodomain has been elucidated by 1H-NMR and restrained modeling. The TTF-1
homeodomain folds in the same manner as classical homeodomains, with three
helices, a loose loop between the first two helices, and a tight turn between
helix II and helix III. The typical assembly of the hydrophobic core is
maintained and N-capping motifs are identified in helix I and helix III. The
N-terminal stretch of helix II exhibits some mobility, similar to the preceding
loop region, which may be related to its anomalous capping. The N-terminal
decapeptide and the C-terminal octapeptide of the molecule (68 residues long)
are disordered. All the previous characteristics are shared by all known
isolated homeodomain structures. An important difference among these structures
occurs at the C-terminal extension of helix III, which is either disordered or
helically folded. In the TTF-1 homeodomain, the C-terminal extension of helix
III (residues 51-59) appears structured, albeit not as rigidly as the preceding
portion. Analysis of the NOEs and hydrogendeuterium exchange of backbone amides
provides evidence for discontinuity between the two moieties of helix III, which
is introduced by a tightening or a kink of residues 51-53.
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
 |
| |
PubMed id
|
 |
Reference
|
 |
|
|
|
 |
A.Carré,
G.Szinnai,
M.Castanet,
S.Sura-Trueba,
E.Tron,
I.Broutin-L'Hermite,
P.Barat,
C.Goizet,
D.Lacombe,
M.L.Moutard,
C.Raybaud,
C.Raynaud-Ravni,
S.Romana,
H.Ythier,
J.Léger,
and
M.Polak
(2009).
Five new TTF1/NKX2.1 mutations in brain-lung-thyroid syndrome: rescue by PAX8 synergism in one case.
|
| |
Hum Mol Genet,
18,
2266-2276.
|
 |
|
|
|
|
 |
C.Genis,
P.Scone,
H.Kasahara,
and
H.J.Nam
(2008).
Crystallization and preliminary X-ray analysis of the NKX2.5 homeodomain in complex with DNA.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
1079-1082.
|
 |
|
|
|
|
 |
D.Gümral,
L.Nadalin,
A.Corazza,
F.Fogolari,
G.Damante,
P.Viglino,
and
G.Esposito
(2008).
Helix mobility and recognition function of the rat thyroid transcription factor 1 homeodomain - hints from 15N-NMR relaxation studies.
|
| |
FEBS J,
275,
435-448.
|
 |
|
|
|
|
 |
P.Del Vecchio,
P.Carullo,
G.Barone,
B.Pagano,
G.Graziano,
A.Iannetti,
R.Acquaviva,
A.Leonardi,
and
S.Formisano
(2008).
Conformational stability and DNA binding energetics of the rat thyroid transcription factor 1 homeodomain.
|
| |
Proteins,
70,
748-760.
|
 |
|
|
|
|
 |
A.Corazza,
C.Rosano,
K.Pagano,
V.Alverdi,
G.Esposito,
C.Capanni,
F.Bemporad,
G.Plakoutsi,
M.Stefani,
F.Chiti,
S.Zuccotti,
M.Bolognesi,
and
P.Viglino
(2006).
Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus.
|
| |
Proteins,
62,
64-79.
|
 |
|
PDB codes:
|
 |
|
|
|
|
|
 |
A.V.D'Elia,
C.Puppin,
L.Pellizzari,
A.Pianta,
E.Bregant,
R.Lonigro,
G.Tell,
F.Fogolari,
V.van Heyningen,
and
G.Damante
(2006).
Molecular analysis of a human PAX6 homeobox mutant.
|
| |
Eur J Hum Genet,
14,
744-751.
|
 |
|
|
|
|
 |
J.E.Ploski,
M.K.Shamsher,
and
A.Radu
(2004).
Paired-type homeodomain transcription factors are imported into the nucleus by karyopherin 13.
|
| |
Mol Cell Biol,
24,
4824-4834.
|
 |
|
|
|
|
 |
E.J.Stollar,
U.Mayor,
S.C.Lovell,
L.Federici,
S.M.Freund,
A.R.Fersht,
and
B.F.Luisi
(2003).
Crystal structures of engrailed homeodomain mutants: implications for stability and dynamics.
|
| |
J Biol Chem,
278,
43699-43708.
|
 |
|
PDB codes:
|
 |
|
|
|
|
|
 |
G.Verdone,
A.Corazza,
P.Viglino,
F.Pettirossi,
S.Giorgetti,
P.Mangione,
A.Andreola,
M.Stoppini,
V.Bellotti,
and
G.Esposito
(2002).
The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition.
|
| |
Protein Sci,
11,
487-499.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
A.V.D'Elia,
G.Tell,
I.Paron,
L.Pellizzari,
R.Lonigro,
and
G.Damante
(2001).
Missense mutations of human homeoboxes: A review.
|
| |
Hum Mutat,
18,
361-374.
|
 |
|
|
|
|
 |
T.Sprules,
N.Green,
M.Featherstone,
and
K.Gehring
(2000).
Conformational changes in the PBX homeodomain and C-terminal extension upon binding DNA and HOX-derived YPWM peptides.
|
| |
Biochemistry,
39,
9943-9950.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
G.Tell,
R.Acquaviva,
S.Formisano,
F.Fogolari,
C.Pucillo,
and
G.Damante
(1999).
Comparative stability analysis of the thyroid transcription factor 1 and Antennapedia homeodomains: evidence for residue 54 in controlling the structural stability of the recognition helix.
|
| |
Int J Biochem Cell Biol,
31,
1339-1353.
|
 |
|
|
|
|
 |
J.P.Schneider,
A.Lombardi,
and
W.F.DeGrado
(1998).
Analysis and design of three-stranded coiled coils and three-helix bundles.
|
| |
Fold Des,
3,
R29-R40.
|
 |
|
 |
 |
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
|
');
}
}
 |